Recombinant SARS-CoV-2 NSP16 [GST] (DAGC199)

Recombinant SARS-CoV-2 NSP16 from E. coli [GST]

Product Overview
Recombinant SARS-CoV-2 NSP16 is produced by E.coli expression system and the target gene encoding Ser6799-Asn7096 is expressed with N-GST Tag.
Target
SARS-CoV-2 NSP16
Nature
Recombinant
Tag/Conjugate
GST
Molecular Weight
Predicted molecular weight 61kDa
Alternative Names
SARS-CoV-2 NSP16; SARS-CoV-2
Procedure
None
Purity
> 90 % as determined by SDS-PAGE.
Format
Liquid
Buffer
Supplied as solution form in PBS, pH 7.5, 0.02% NLS
Preservative
None
Storage
Use a manual defrost freezer and avoid repeated freeze thaw cycles. Store at 2 to 8°C for one week. Store at -20 to -80°C for twelve months from the date of receipt.
Introduction
NSP10, Plays a pivotal role in viral transcription by stimulating both nsp14 3'-5' exoribonuclease and 2'-O-methyltransferase (NSP16) activities. Therefore plays an essential role in viral mRNAs cap methylation. 2'-O-methyltransferase (NSP16) that mediates mRNA cap 2'-O-ribose methylation to the 5'-cap structure of viral mRNAs. N7-methyl guanosine cap is a prerequisite for binding of nsp16. Therefore plays an essential role in viral mRNAs cap methylation which is essential to evade immune system. Nsp10 forms a dodecamer and interacts with nsp14 and nsp16; these interactions enhance nsp14 and nsp16 enzymatic activities.
Keywords
SARS-CoV-2 NSP16; SARS-CoV-2

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References


Ilimaquinone (marine sponge metabolite) as a novel inhibitor of SARS-CoV-2 key target proteins in comparison with suggested COVID-19 drugs: designing, docking and molecular dynamics simulation study

RSC ADVANCES

Authors: Surti, Malvi; Patel, Mitesh; Adnan, Mohd; Moin, Afrasim; Ashraf, Syed Amir; Siddiqui, Arif Jamal; Snoussi, Mejdi; Deshpande, Sumukh; Reddy, Mandadi Narsimha

The outbreak of novel coronavirus, SARS-CoV-2, has infected more than 36 million people and caused approximately 1 million deaths around the globe as of 9 October 2020. The escalating outspread of the virus and rapid rise in the number of cases require the instantaneous development of effectual drugs and vaccines. Presently, there are no approved drugs or vaccine available to treat the infection. In such scenario, one of the propitious therapeutic approaches against viral infection is to explore enzyme inhibitors amidst natural compounds, utilizing computational approaches aiming to get products with negligible side effects. In the present study, the inhibitory prospects of ilimaquinone (marine sponge metabolite) were assessed in comparison with hydroxychloroquine, azithromycin, favipiravir, ivermectin and remdesivir at the active binding pockets of nine different vital SARS-CoV-2 target proteins (spike receptor binding domain, RNA-dependent RNA polymerase, Nsp10, Nsp13, Nsp14, Nsp15, Nsp16, main protease, and papain-like-protease), employing an in silico molecular interaction based approach. In addition, molecular dynamics (MD) simulations of the SARS-CoV-2 papain-like protease (PLpro)-ilimaquinone complex were also carried out to calculate various structural parameters including root mean square fluctuation (RMSF), root mean square deviation (RMSD), radius of gyration (R-g) and hydrogen bond interactions. PLpro is a promising drug target, due to its imperative role in viral replication and additional function of stripping ubiquitin and interferon-stimulated gene 15 (ISG15) from host-cell proteins. In light of the possible inhibition of all vital SARS-CoV-2 target proteins, our study has emphasized the importance to study in depth ilimaquinone actions in vivo.

H-1, C-13, and N-15 backbone chemical shift assignments of coronavirus-2 non-structural protein Nsp10

BIOMOLECULAR NMR ASSIGNMENTS

Authors: Kubatova, N.; Qureshi, N. S.; Altincekic, N.; Abele, R.; Bains, J. K.; Ceylan, B.; Ferner, J.; Fuks, C.; Hargittay, B.; Hutchison, M. T.; de Jesus, V.; Kutz, F.; Wirtz Martin, M. A.; Meiser, N.; Linhard, V.; Pyper, D. J.; Trucks, S.; Furtig, B.; Hengesbach, M.; Lohr, F.; Richter, C.; Saxena, K.; Schlundt, A.; Schwalbe, H.; Sreeramulu, S.; Wacker, A.; Weigand, J. E.; Wirmer-Bartoschek, J.; Woehnert, J.

The international Covid19-NMR consortium aims at the comprehensive spectroscopic characterization of SARS-CoV-2 RNA elements and proteins and will provide NMR chemical shift assignments of the molecular components of this virus. The SARS-CoV-2 genome encodes approximately 30 different proteins. Four of these proteins are involved in forming the viral envelope or in the packaging of the RNA genome and are therefore called structural proteins. The other proteins fulfill a variety of functions during the viral life cycle and comprise the so-called non-structural proteins (nsps). Here, we report the near-complete NMR resonance assignment for the backbone chemical shifts of the non-structural protein 10 (nsp10). Nsp10 is part of the viral replication-transcription complex (RTC). It aids in synthesizing and modifying the genomic and subgenomic RNAs. Via its interaction with nsp14, it ensures transcriptional fidelity of the RNA-dependent RNA polymerase, and through its stimulation of the methyltransferase activity of nsp16, it aids in synthesizing the RNA cap structures which protect the viral RNAs from being recognized by the innate immune system. Both of these functions can be potentially targeted by drugs. Our data will aid in performing additional NMR-based characterizations, and provide a basis for the identification of possible small molecule ligands interfering with nsp10 exerting its essential role in viral replication.

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